4FH1: S. cerevisiae Ubc13-N79A

S. cerevisiae Ubc13-N79A. Determined by X-ray diffraction at 2.61 Å resolution. Released 9 Jan 2013.

Method: X-ray diffraction
Resolution: 2.61 Å
Organism: Saccharomyces cerevisiae
Chains: 1
Atoms: 1,130
Mol. weight: 17.64 kDa
Ligands: NHE
Released: 9 Jan 2013

Explore 4FH1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4FH1 contains 8 α-helices and 9 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 8 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	6-17	12
α-helix	19-20	2
β-strand	23-28	6	1
β-strand	31-40	10	1
α-helix	41-42	2
β-strand	50	1	2
β-strand	51-57	7	1
α-helix	66-67	2
β-strand	68-71	4	1
β-strand	77	1	3
β-strand	80	1	3
β-strand	86	1	3
α-helix	89-91	3
α-helix	101-113	13
α-helix	125-128	4
α-helix	133-147	15
β-strand	150	1	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin-conjugating enzyme E2 13	A	protein	153	Saccharomyces cerevisiae	P52490 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4FH1_1 Ubiquitin-conjugating enzyme E2 13 (chains A)
MASLPKRIIKETEKLVSDPVPGITAEPHDDNLRYFQVTIEGPEQSPYEDGIFELELYLPD
DYPMEAPKVRFLTKIYHPAIDRLGRISLDVLKTNWSPALQIRTVLLSIQALLASPNPNDP
LANDVAEDWIKNEQGAKAKAREWTKLYAKKKPE

Ligands and cofactors

ID	Name	Formula	Copies
NHE	2-[N-cyclohexylamino]ethane sulfonic acid	C8 H17 N O3 S	1

Primary citation

A conserved asparagine has a structural role in ubiquitin-conjugating enzymes. Berndsen, C.E., Wiener, R., Yu, I.W. et al. Nat Chem Biol (2013) 9:154-156. DOI 10.1038/nchembio.1159 · PubMed

Other PDB entries of the same protein (UniProt P52490 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9GLT 1.45 Å, Crystal Structure of Yeast Ubc13 C87E
1JAT 1.6 Å, Mms2/Ubc13 Ubiquitin Conjugating Enzyme Complex
1JBB 2.0 Å, Ubiquitin Conjugating Enzyme, Ubc13
5OJW 2.0 Å, S. cerevisiae UBC13 - MMs2 complex
6ZHT 2.3 Å, Uba1-Ubc13 disulfide mediated complex
6ZHS 2.35 Å, Uba1 bound to two E2 (Ubc13) molecules
2GMI 2.5 Å, Mms2/Ubc13~Ubiquitin

Browse structure collections

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